Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Denatured-state ensemble and the early-stage folding of the G29A mutant of the B-domain of protein A.

The journal of physical chemistry. B - 12 May 2005

Chowdhury Shibasish, Lei Hongxing, Duan Yong

Abstract excerpt

The folding mechanism of the G29A mutant of the B-domain of protein A (BdpA) has been studied by all-atom molecular dynamics simulation using AMBER force field (ff03) and generalized Born continuum solvent model. Started from the extended chain conformation, a total of 16 simulations (400 ns each) at 300 K captured some early folding events of the G29A mutant of BdpA. In one of the 16 trajectories, the G29A...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cluster Analysis
Share to Hydrogen Bonding
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Denaturation

Share to Staphylococcal Protein A

Source

Identifiers

PMID: 16852080
DOI: 10.1021/jp0449814

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Denatured-state ensemble and the early-stage folding of the G29A mutant of the B-domain of protein A.PMID 16852080Read ↗

Folding processes of the B domain of protein A to the native state observed in all-atom ab initio folding simulations.Semantic proximity Read ↗

Preventing fibril formation of a protein by selective mutation.Semantic proximity Read ↗

Effects of mutation, truncation, and temperature on the folding kinetics of a WW domain.Semantic proximity Read ↗

Testing protein-folding simulations by experiment: B domain of protein A.Semantic proximity Read ↗

Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.Semantic proximity Read ↗

The role of plastic beta-hairpin and weak hydrophobic core in the stability and unfolding of a full sequence design protein.Semantic proximity Read ↗

Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A.Semantic proximity Read ↗

The protein folding network indicates that the ultrafast folding mutant of villin headpiece subdomain has a deeper folding funnel.Semantic proximity Read ↗

Probing the folding intermediate of Rd-apocyt b562 by protein engineering and infrared T-jump.Semantic proximity Read ↗

An on-pathway hidden intermediate and the early rate-limiting transition state of Rd-apocytochrome b562 characterized by protein engineering.Semantic proximity Read ↗

DBFOLD: An efficient algorithm for computing folding pathways of complex proteinsSemantic proximity Read ↗

A topologically conserved aliphatic residue in alpha-helix 6 stabilizes the hydrophobic core in domain II of glutathione transferases and is a structural determinant for the unfolding pathway.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.